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FPR4 peptidylprolyl isomerase FPR4 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851170, updated on 2-Nov-2024

Summary

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Official Symbol
FPR4
Official Full Name
peptidylprolyl isomerase FPR4
Primary source
SGD:S000004441
Locus tag
YLR449W
See related
AllianceGenome:SGD:S000004441; FungiDB:YLR449W; VEuPathDB:YLR449W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables macrolide binding activity and peptidyl-prolyl cis-trans isomerase activity. Involved in nucleosome assembly. Acts upstream of or within maintenance of rDNA. Located in chromatin and nucleus. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See FPR4 in Genome Data Viewer
Location:
chromosome: XII
Exon count:
1
Sequence:
Chromosome: XII; NC_001144.5 (1030834..1032012)

Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene H(+)-transporting V0 sector ATPase subunit d Neighboring gene ribosomal 60S subunit protein L6B Neighboring gene hydroxymethylglutaryl-CoA reductase (NADPH) HMG2 Neighboring gene leucine-responsive transcriptional regulator LEU3

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p. Monneau YR, et al. Biomol NMR Assign, 2012 Oct. PMID 21898050
  2. Intrinsic disorder of a nucleoplasmin-like histone chaperone specifies its discrete nuclear and nucleolar functions. Gauthier CM, et al. FEBS Lett, 2024 Jan. PMID 38058218
  3. The FK506-binding protein, Fpr4, is an acidic histone chaperone. Xiao H, et al. FEBS Lett, 2006 Aug 7. PMID 16846601
  4. A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing. Kuzuhara T, et al. Nat Struct Mol Biol, 2004 Mar. PMID 14981505
  5. Basic surface features of nuclear FKBPs facilitate chromatin binding. Leung A, et al. Sci Rep, 2017 Jun 19. PMID 28630422, Free PMC Article

See all (95) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The results thus provide a further demonstration for the elusive role of Fpr3 and Fpr4 in histone chaperones.
    Title: Nuclear FKBPs, Fpr3 and Fpr4 affect genome-wide genes transcription.
  2. Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization.
    Title: Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables macrolide binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidyl-prolyl cis-trans isomerase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptidyl-prolyl cis-trans isomerase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidyl-prolyl cis-trans isomerase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within maintenance of rDNA IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nucleosome assembly IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in chromatin IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in chromatin IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleolus HDA PubMed 
is_active_in nucleolus IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
peptidylprolyl isomerase FPR4
NP_013554.3
  • Nuclear peptidyl-prolyl cis-trans isomerase (PPIase); impacts expression of multiple genes via its role in nucleosome assembly; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones; role in rDNA maintenance; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; contains a nucleoplasmin-like fold and can form pentamers

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001144.5 Reference assembly

    Range
    1030834..1032012
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182337.3 → NP_013554.3  TPA: peptidylprolyl isomerase FPR4 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013554.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VZ83, Q06205
    UniProtKB/TrEMBL
    A7A1W8, B3RHV7, B5VNY5, C8ZE56, N1P7H6
    Conserved Domains (2) summary
    COG0545
    Location:275 → 392
    FkpA; FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]
    pfam17800
    Location:10 → 164
    NPL; Nucleoplasmin-like domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q06205.1

Gene LinkOut

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